Abstract
The occurrence of hydrogenosomes in independent eukaryotic lineages implies that they evolved from mitochondrial predecessors which most likely were already highly diverse in functional range and protein content. In contrast to mitochondria, where multiple large-scale genome and proteome analyses provide a constantly increasing coverage of organellar protein content and functions, hydrogenosomes are mostly described by small-scale studies on single proteins or pathways in a very small number of organisms to date. Several independent analyses can be drawn upon to compile a preliminary inventory of the hydrogenosomal proteome in trichomonads: multiple experimental studies on single proteins or pathways, gene products predicted by a computer algorithm to contain an N-terminal targeting peptide for import into hydrogenosomes, and proteins identified by a proteomic approach based on 2D electrophoresis of purified hydrogenosomes. On the basis of these observations the proteome of T. vaginalis hydrogenosomes can be tentatively estimated to consist of at least about 200 different proteins, but certainly significantly less than the 700 proteins predicted for yeast mitochondria. This estimate puts the trichomonad organelles in the range of the highly reduced mitochondria in parasitic organisms or mitosomes.
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Henze, K. (2007). The Proteome of T. vaginalis Hydrogenosomes. In: Tachezy, J. (eds) Hydrogenosomes and Mitosomes: Mitochondria of Anaerobic Eukaryotes. Microbiology Monographs, vol 9. Springer, Berlin, Heidelberg. https://doi.org/10.1007/7171_2007_106
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DOI: https://doi.org/10.1007/7171_2007_106
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